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EC Tree
IUBMB Comments A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).
The taxonomic range for the selected organisms is: Canis lupus familiaris The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sult1a1, sult2a1, sult1e1, sulphotransferase, sult1a3, phenol sulfotransferase, cytosolic sulfotransferase, sult4a1, sult1b1, sult1a2,
more
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1-naphthol phenol sulfotransferase
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-
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2-naphtholsulfotransferase
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-
-
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4-nitrocatechol sulfokinase
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-
-
-
arylsulfotransferase
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-
-
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catecholamine-sulfating phenol sulfotransferase
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-
-
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DOPA/tyrosine sulfotransferase
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-
-
-
dopamine sulfotransferase
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-
-
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hippocampal phenol sulfotransferase
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-
-
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minoxidil sulfotransferase
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-
-
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monoamine sulfotransferase
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-
-
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p-nitrophenol sulfotransferase
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phenol sulfokinase
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phenol sulfotransferase
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phenol/aryl sulfotransferase
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ritodrine sulfotransferase
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sulfotransferase, aryl
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sulfotransferase, monoamine-preferring
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thermolabile phenol sulfotransferase
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thermostable phenol sulfotransferase
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tyrosine-ester sulfotransferase
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3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate
mechanism
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sulfate group transfer
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-
-
-
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3'-phosphoadenylyl-sulfate:phenol sulfotransferase
A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).
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3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylylsulfate + beta-estradiol
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-hydroxyestradiol
adenosine 3',5'-bisphosphate + estradiol 2-sulfate
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-
-
-
?
3'-phosphoadenylylsulfate + 2-hydroxyestrone
adenosine 3',5'-bisphosphate + estrone 2-sulfate
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-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylylsulfate + adrenaline
adenosine 3',5'-bisphosphate + adrenaline sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + norepinephrine
adenosine 3',5'-bisphosphate + norepinephrine sulfate
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i.e. noradrenalin
i.e. noradrenalin sulfate
?
additional information
?
-
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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-
r
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
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-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
SULT1A1
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-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
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-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
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-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
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enzyme form SULT1D1
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-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
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-
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
enzyme form SULT1D1
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-
?
additional information
?
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?
additional information
?
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-
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?
additional information
?
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no activity with dehydroepiandrosterone
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-
?
additional information
?
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no activity with dehydroepiandrosterone
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?
additional information
?
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different enzyme forms show overlapping substrate specificities, overview
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?
additional information
?
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isoenzyme B catalyzes the sulfurylation of a wider range of substrates than A which is preferentially active with dopamine
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-
?
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1-naphthol
SULT1A1, substrate inhibition at 0.0005 mM
4-nitrophenol
SULT1A1, substrate inhibition at 0.001 mM
4-nitrophenol
-
substrate inhibition, enzyme form SULT1D1
dopamine
-
substrate inhibition, enzyme form SULT1D1
KCl
-
50 mM, 60% inhibition of isoenzyme A, slight activation of isoenzyme B
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EDTA
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10 mM, stimulates isozymes A and B
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0.000069 - 0.00015
4-nitrophenol
0.014
beta-estradiol
SULT1A1, pH 7.3-7.4
0.55
minoxidil
SULT1A1, pH 7.3-7.4
0.0017 - 0.026
3'-phosphoadenylylsulfate
0.0015 - 1.6
4-nitrophenol
additional information
additional information
kinetics
-
0.000069
4-nitrophenol
SULT1A1, pH 7.3-7.4
0.00015
4-nitrophenol
SULT1A1, pH 7.0
0.175
dopamine
SULT1A1, pH 7.0
0.18
dopamine
SULT1A1, pH 7.3-7.4
0.0017
3'-phosphoadenylylsulfate
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with dopamine, isoenzyme A, pH 6.0, 37°C
0.026
3'-phosphoadenylylsulfate
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with dopamine, isoenzyme B, pH 9.5, 37°C
0.0015
4-nitrophenol
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mutant enzyme D247L, enzyme form SULT1D1
0.18
4-nitrophenol
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wild-type enzyme, enzyme form SULT1D1
1.6
4-nitrophenol
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mutant enzyme O86D, enzyme form SULT1D1
0.0036
dopamine
-
wild-type enzyme, enzyme form SULT1D1
0.0062
dopamine
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isoenzyme B, pH 9.5, 37°C
0.0177
dopamine
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isoenzyme A, pH 6.0, 37°C
0.031
dopamine
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mutant enzyme D247L, enzyme form SULT1D1
0.037
dopamine
-
mutant enzyme O86D, enzyme form SULT1D1
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0.026 - 0.15
4-nitrophenol
0.026
4-nitrophenol
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mutant enzyme D247L, enzyme form SULT1D1
0.089
4-nitrophenol
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mutant enzyme O86D, enzyme form SULT1D1
0.15
4-nitrophenol
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wild-type enzyme, enzyme form SULT1D1
0.028
dopamine
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mutant enzyme D247L, enzyme form SULT1D1
0.09
dopamine
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mutant enzyme O86D, enzyme form SULT1D1
0.18
dopamine
-
wild-type enzyme, enzyme form SULT1D1
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0.061
dopamine
-
substrate inhibition, wild-type enzyme, enzyme form SULT1D1
0.063
4-nitrophenol
-
substrate inhibition, mutant enzyme D247L, enzyme form SULT1D1
1
4-nitrophenol
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substrate inhibition, wild-type enzyme, enzyme form SULT1D1
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0.0016
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purified isozyme A
0.0036
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purified isozyme B
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5.5
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with substrate 4-nitrophenol, isoenzyme B
6
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with substrate dopamine, isoenzyme A
9.5
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with substrate dopamine, isoenzyme B
6.5
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isoenzyme A
6.5
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with substrate 4-nitrophenol
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additional information
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P-PST, 100% identical in amino acid sequence with GenBank accession number AY069922
SwissProt
brenda
ST1A7
SwissProt
brenda
SULT1A1, 100% identical in amino acid sequence with GenBank accession number D29807
SwissProt
brenda
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SULT1A1
brenda
SULT1A1, higher content in male than in female dogs
brenda
SULT1A1
brenda
SULT1A1
brenda
SULT1A1
brenda
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-
brenda
-
brenda
SULT1A1
brenda
higher content in male than in female dogs
brenda
-
brenda
SULT1A1
brenda
higher content in male than in female dogs
brenda
-
brenda
SULT1A1
brenda
higher content in male than in female dogs
brenda
-
brenda
SULT1A1
brenda
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SULT1A1
brenda
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ST1A1_CANLF
295
0
34115
Swiss-Prot
other Location (Reliability: 2 )
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A146D
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sulfation activity of the mutant is strongly decreased for the substrates 4-nitrophenol and dopamine, enzyme form SULT1D1
A146Q
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sulfation activity of the mutant is strongly decreased for the substrates 4-nitrophenol and dopamine, enzyme form SULT1D1
D247L
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21fold better sulfation of 4-nitrophenol (120fold decrease in KM-value) and 54fold less efficient in sulfation of dopamine (8fold increase in KM-value) compared to wild-type enzyme. Preference is switched from dopamine to 4-nitrophenol, enzyme form SULT1D1
I86D
-
sulfation activity of the mutant is strongly decreased for the substrates 4-nitrophenol and dopamine, enzyme form SULT1D1
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recombinant His-tagged enzyme from Escherichia coli
isozyme A 18fold, isozyme B 35fold
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DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli BL21(DE3) as His-tagged protein
wild-type and mutant enzymes
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Romain, Y.; Demassieux, S.; Carriere, S.
Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines
Biochem. Biophys. Res. Commun.
106
999-1005
1982
Canis lupus familiaris
brenda
Tsoi, C.; Morgenstern, R.; Swedmark, S.
Canine sulfotransferase SULT1A1: molecular cloning, expression, and characterization
Arch. Biochem. Biophys.
401
125-133
2002
Canis lupus familiaris (Q29476), Canis lupus familiaris
brenda
Duffel, M.W.; Marshall, A.D.; McPhie, P.; Sharma, V.; Jakoby, W.B.
Enzymatic aspects of the phenol (aryl) sulfotransferases
Drug Metab. Rev.
33
369-395
2001
Bos taurus, Homo sapiens, Homo sapiens (O00338), Homo sapiens (O43704), Homo sapiens (O75897), Mus musculus, Mus musculus (Q3UZZ6), Mus musculus (Q80VR3), Mus musculus (Q9QWG7), Rattus norvegicus, Rattus norvegicus (P50237), Rattus norvegicus (P52847), Rattus norvegicus (Q9WUW8), Rattus norvegicus (Q9WUW9), Oryctolagus cuniculus (O46503), Oryctolagus cuniculus (Q9XT99), Macaca fascicularis (P52846), Canis lupus familiaris (Q29476), Oryctolagus cuniculus ST1A8 (Q9XT99), Oryctolagus cuniculus ST1C5 (O46503), Mus musculus ST1c4 (Q80VR3), Macaca fascicularis ST1A9 (P52846), Mus musculus ST1a4
brenda
Tsoi, C.; Widersten, M.; Morgenstern, R.; Swedmark, S.
Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity
Biochem. J.
378
687-692
2004
Canis lupus familiaris
brenda